Cadherins comprise a large family of cell adhesion molecules (CAMs) that mediate cell-cell adhesion. The type I classical cadherins, which include epithelial (E)-cadherin and neuronal (N)-cadherin, are homophilic, calcium-dependent CAMs. Although originally identified based on the cell type in which they were discovered, both E- and N-cadherin are found throughout the body. N-cadherin stabilizes cell-cell adhesions at neuronal synapses but also promotes cell migration during tissue morphogenesis and neuronal growth cone guidance. Structurally, type I cadherins have five extracellular cadherin (EC) domain repeats, a transmembrane segment and a highly conserved cytoplasmic segment. The site of homophilic binding lies in the distal-most EC domain, EC1. Both the His-Ala-Val (HAV) sequence (SEQ ID NO: 1) and the Trp2 residue are unique to classical cadherins and regulate homophilic binding. In fact, both peptides and cyclic peptides that comprise the HAV sequence of N-cadherin are sufficient to disrupt cell-cell adhesion and neurite outgrowth. Atypical (type II) cadherins, such as Cadherin-11, also have cell adhesion recognition sequences that have been identified and can be targeted in a similar fashion.